View source for 7lgj


==Cyanophycin synthetase 1 from Synechocystis sp. UTEX2470 with ADPCP and 8x(Asp-Arg)-NH2==
<StructureSection load='7lgj' size='340' side='right'caption='[[7lgj]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7lgj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6714 Synechocystis sp. PCC 6714] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7ID:(2~{S})-2-[[(3~{S})-3-azanyl-4-oxidanyl-4-oxidanylidene-butanoyl]amino]-5-carbamimidamido-pentanoic+acid'>7ID</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7lgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lgj OCA], [https://pdbe.org/7lgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lgj RCSB], [https://www.ebi.ac.uk/pdbsum/7lgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lgj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A068N621_SYNY4 A0A068N621_SYNY4] Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).[ARBA:ARBA00003184]
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== Publication Abstract from PubMed ==
Cyanophycin is a natural biopolymer produced by a wide range of bacteria, consisting of a chain of poly-L-Asp residues with L-Arg residues attached to the beta-carboxylate sidechains by isopeptide bonds. Cyanophycin is synthesized from ATP, aspartic acid and arginine by a homooligomeric enzyme called cyanophycin synthetase (CphA1). CphA1 has domains that are homologous to glutathione synthetases and muramyl ligases, but no other structural information has been available. Here, we present cryo-electron microscopy and X-ray crystallography structures of cyanophycin synthetases from three different bacteria, including cocomplex structures of CphA1 with ATP and cyanophycin polymer analogs at 2.6 A resolution. These structures reveal two distinct tetrameric architectures, show the configuration of active sites and polymer-binding regions, indicate dynamic conformational changes and afford insight into catalytic mechanism. Accompanying biochemical interrogation of substrate binding sites, catalytic centers and oligomerization interfaces combine with the structures to provide a holistic understanding of cyanophycin biosynthesis.

Structures and function of the amino acid polymerase cyanophycin synthetase.,Sharon I, Haque AS, Grogg M, Lahiri I, Seebach D, Leschziner AE, Hilvert D, Schmeing TM Nat Chem Biol. 2021 Oct;17(10):1101-1110. doi: 10.1038/s41589-021-00854-y. Epub, 2021 Aug 12. PMID:34385683<ref>PMID:34385683</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6714]]
[[Category: Synthetic construct]]
[[Category: Grogg M]]
[[Category: Hilvert D]]
[[Category: Schmeing TM]]
[[Category: Sharon I]]